1.14.13.236 | physiological function |
proteins required for the in Vitro reconstitution of T4MO catalytic activity are a diiron hydroxylase (T4MOH), a Rieske-type ferredoxin (T4MOC), an effector protein (T4MOD), and an NADH oxidoreductase (T4MOF). The T4MOH component is composed of the tmoA, tmoB, and tmoE gene products with quaternary structure (alpha,beta,epsilon)2. T4MOH is the hydroxylase, the NADH-dependent multiple-turnover hydroxylation activity is increased by more than 100fold in the presence of T4MOC, which mediates highly specific electron transfer between T4MOF and T4MOH. T4MOD is a 11.6 kDa monomeric protein devoid of cofactors or redox-active metal ions and is also detected as a substoichiometric consitutent of the purified T4MOH. The rate of the hydroxylation reaction can be mildly stimulated by the further addition of separately purified T4MOD to the T4MOH |
-, 740033 |